Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation-Reference-Cited by-同舟云学术

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

Published:2017-06-29 Issue:1 Volume:8 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Afroz Tariq,Hock Eva-Maria,Ernst Patrick,Foglieni Chiara,Jambeau Melanie,Gilhespy Larissa A. B.,Laferriere Florent,Maniecka Zuzanna,Plückthun Andreas,Mittl Peer,Paganetti Paolo^ORCID,Allain Frédéric H. T.,Polymenidou Magdalini

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-017-00062-0.pdf

Reference61 articles.

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3. Buratti, E. & Baralle, F. E. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J. Biol. Chem. 276, 36337–36343 (2001).

4. Arai, T. et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 351, 602–611 (2006).

5. Hock, E. M. & Polymenidou, M. Prion-like propagation as a pathogenic principle in frontotemporal dementia. J. Neurochem. 138(Suppl 1): 163–183 (2016).

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